Linked Life Data

7931272

Source:http://linkedlifedata.com/resource/pubmed/id/7931272

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1994-11-1
pubmed:abstractText
The hallmark event of Alzheimer's disease (AD) is the deposition of amyloid as insoluble fiber masses in extracellular neuritic plaques and around the walls of cerebral blood vessels. The main component of amyloid is a hydrophobic peptide, named amyloid beta-peptide (beta A4), which results from the processing of a much longer membrane amyloid precursor protein (APP). This review focuses on the structural features of beta A4 and the factors that determine beta A4 insolubilization. Theoretical and experimental studies of the primary structure of beta A4 have shown that it is composed of a completely hydrophobic C-terminal domain, which adopts beta-strand structure, and an N-terminal region, whose sequence permits different secondary structures. In fact, this region can exist as an alpha-helical or beta-strand conformation depending on the environmental condition (pH and hydrophobicity surrounding the molecule). The effects of pH and hydrophobicity on beta A4 structure may elucidate the mechanisms determining its aggregation and amyloid deposition in AD.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-3042
pubmed:author
pubmed:issnType
Print
pubmed:volume
63
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1191-8
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Structural determinants of the Alzheimer's amyloid beta-peptide.
pubmed:affiliation
Departamento de Biología Celular y Molecular, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Santiago.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't